Pre-treatment with beta-arrestin2 agonists was shown to inhibit the AMPK/mTOR signaling pathway, and to inhibit autophagy by restoring the levels of beta-arrestin2 in BEAS-2B cells. These changes were reversed with the knockdown of beta-arrestin2, indicating that beta-arrestin2 suppressed autophagy through the AMPK-mTOR signaling pathway.

These results show that b-arrestin1 and b-arrestin2 exert differential actions on PAC1R internalization and PAC1R-dependent ERK1/2 activation, and suggest that the two b-arrestin isoforms may be involved in fine and precise tuning of the PAC1R signaling pathways.

overexpression of beta-arrestin2 can inhibit the growth of renal cell carcinoma (RCC) cells in vitro, and beta-arrestin2 acts as a tumor suppressor gene in RCC; the main mechanism may directly suppress the phosphorylation of IkBa and indirectly suppress NFkB

Study investigated the association between five ARRB2 single nucleotide polymorphisms (SNPs): rs1045280, rs2036657, rs4790694, rs3786047 and rs452246, and response to antidepressant treatment in a sample of 569 patients with a major depressive episode treated for 6months: GG/GT patients for rs4522461 and AA/AC patients for rs4790694 had a lower response.

Itch/beta-arrestin2 complex binds SuFu and induces its Lys63-linked polyubiquitylation without affecting its stability.

These data highlight a novel arrestin-mediated modulation of CREB signalling, suggesting a reciprocal relationship between arrestin2 and arrestin3, wherein recruitment of arrestin3 restricts the ability of beta2AR to activate prolonged CREB phosphorylation by precluding recruitment of an arrestin2/Src/p38 complex.

A novel regulatory role of GRK2 was proposed for the ubiquitination of beta-arrestin in the context of the PKC-mediated heterologous regulation of GPCRs.

Data indicate that a constitutively monomeric CXCL12 variant reproduced the G protein-dependent and beta-arrestin-dependent responses that are associated with normal CXCR4 signaling and lead to cell migration.

This work demonstrates that the expression of FSHR and LHCGR can be induced in hGL5 cells but that the FSHR-dependent cAMP/PKA pathway is constitutively silenced, possibly to protect cells from FSHR-cAMP-PKA-induced apoptosis.

Lowering the level of cellular FLNA caused an elevation in RalA activity and resulted in selective interference with the normal intracellular trafficking and signaling of D3R through beta-arrestins.

This study reveals contrasting abilities of IGF-1R to interact with each b-arrestin isoform, depending on the presence of the ligand and demonstrates the antagonism between the two b-arrestin isoforms in controlling IGF-1R expression and function, which could be developed into a practical anti-IGF-1R strategy for cancer therapy.

Results demonstrate that GPR3 signals at the plasma membrane and can be silenced by GRK2/beta-arrestin overexpression. These results also strongly implicate the serine and/or threonine residues in the third intracellular loop in the regulation of GPR3 activity.

AT1R-beta-arrestin-2 pathway signaling plays an important role in renal fibrosis.

These data suggest that one allele of arrestin-2 is unable to support normal locomotor behavior due to signaling and/or developmental defects.

Beta-arrestin-2 with beta-arrestin-1 shared common mechanisms to suppress podocyte autophagy by negative regulation of ATG12-ATG5 conjugation.

[beta]-arrestin2 regulates intestinal mucosal inflammation under both homeostatic and colitic conditions. Its mode of action involves negative regulation of T-cell activation and its requirement for induction of regulatory T cells.

Results suggest that the antipruritic effects of kappa opioid receptor agonists may not require betaarrestin2

that pro- and anti-inflammatory activities of beta-arrestin2 are determined by beta-arrestin2 ubiquitination and that changes in USP20 expression and/or activity can therefore regulate inflammatory responses

Xenopus laevis Arrestin, beta 2 (ARRB2) Interaktionspartner

Arrb2 physically interacts with the beta subunit of trimeric G-proteins and Dishevelled, the interaction between arrb2 and Dishevelled is promoted by the beta/gamma subunits of trimeric G-proteins.

Zebrafish Arrestin, beta 2 (ARRB2) Interaktionspartner

results suggest that a functional interaction between beta-arrestin 2 and Smoothened may be critical to regulate hedgehog signaling in zebrafish development

Arrestin 3 (ARRB2) Protein Überblick

Protein Überblick

Members of arrestin/beta-arrestin protein family are thought to participate in agonist-mediated desensitization of G-protein-coupled receptors and cause specific dampening of cellular responses to stimuli such as hormones, neurotransmitters, or sensory signals. Arrestin beta 2, like arrestin beta 1, was shown to inhibit beta-adrenergic receptor function in vitro. It is expressed at high levels in the central nervous system and may play a role in the regulation of synaptic receptors. Besides the brain, a cDNA for arrestin beta 2 was isolated from thyroid gland, and thus it may also be involved in hormone-specific desensitization of TSH receptors. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.